Table 2 Comparison of the distance between C7 of the indole ring of Trp (W104 in AppABLUF) and N3 of the isoalloxazine ring of flavin from the various crystal structures available for AppABLUF, AppA full-length domains and other BLUF domains.

From: Functional dynamics of a single tryptophan residue in a BLUF protein revealed by fluorescence spectroscopy

Protein

pdb/FRET

Distance (Å)

references

AppABLUF (17–133)

1yrx

5.9

50

AppABLUF (5–125)

2bun

6.2

28

C20S AppABLUF (1–124)

2iyg (dark)

16.0

20

C20S AppABLUF (1–124)

2iyi (light)

16.2

20

C20S AppA Δ399

4hh0

15.7

50

wt AppA Δ399

4hh1

15.7

50

TePixDBLUF (2–143)

1x0p

16.1

21

Slr1694BLUF (2–140)

2hfn

15.7, 5.7*

22

OAPAC (1–366)

4yus

16.6

24

BrlBBLUF (1–140)

2byc

16.0

23

7azaW104W64F AppA (dark)

FRET:FL

20.5

this work

7azaW104W64F AppA (light)

FRET:FL

9.5

this work

7azaW104W64F AppA (dark)

FRET: AEM

17.7

this work

7azaW104W64F AppA (light)

FRET: AEM

8.3

this work

  1. An average distance is provided for those structures that contain more than one subunit. *In Slr1694BLUF (2–140), a shorter distance (5.7 Å) is observed in one of the ten subunits. FRET: FL refers to our FRET measurements using fluorescent lifetimes and FRET: AEM to FRET measurements using the acceptor enhancement method.
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